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Conserved domains on  [gi|224809466|ref|NP_001139266|]
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anthrax toxin receptor 2 isoform 2 precursor [Homo sapiens]

Protein Classification

vWA_ATR and Anth_Ig domain-containing protein( domain architecture ID 10107123)

protein containing domains vWA_ATR, Anth_Ig, and Ant_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 39-221 6.54e-110

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


:

Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 323.31  E-value: 6.54e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  39 CRRAFDLYFVLDKSGSVANNWIEIYNFVQQLAERFVSPEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGET 118
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466 119 YIHEGLKLANEQI--QKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSKEQV 196
Cdd:cd01474   81 YIHEGLENANEQIfnRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|....*
gi 224809466 197 FPVKGGFQALKGIINSILAQSCTEI 221
Cdd:cd01474  161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 216-317 4.28e-56

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


:

Pssm-ID: 461684  Cd Length: 102  Bit Score: 182.06  E-value: 4.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  216 QSCTEILELQPSSVCVGEEFQIVLSGRGFMLGSRNGSVLCTYTVNETYTTSVKPVSVQLNSMLCPAPILNKAGETLDVSV 295
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 224809466  296 SFNGGKSVISGSLIVTATECSN 317
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
Ant_C super family cl05253
Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic ...
 394-479 1.83e-48

Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic C-terminus of the anthrax receptor.


The actual alignment was detected with superfamily member pfam05586:

Pssm-ID: 461683  Cd Length: 93  Bit Score: 161.70  E-value: 1.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  394 VRWGDKGSTEEGARLEKAKNAVVKIPEETEEPIRPRPPRPKPTHQPPQTKWYTPIKGRLDALWALLRRQYDRVSLMRPQE 473
Cdd:pfam05586   1 VRWGEKGSTEEGAKLEKAKNAVVKMPEEEEEPPEPRPRKPPARKPPPQRKWYTPIKGKLDALWALLRRGYDRVSLMRPTP 80


                  ....*..
gi 224809466  474 GDE-VCI 479
Cdd:pfam05586  81 GDKgRCI 87
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 39-221 6.54e-110

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 323.31  E-value: 6.54e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  39 CRRAFDLYFVLDKSGSVANNWIEIYNFVQQLAERFVSPEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGET 118
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466 119 YIHEGLKLANEQI--QKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSKEQV 196
Cdd:cd01474   81 YIHEGLENANEQIfnRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|....*
gi 224809466 197 FPVKGGFQALKGIINSILAQSCTEI 221
Cdd:cd01474  161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 216-317 4.28e-56

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


Pssm-ID: 461684  Cd Length: 102  Bit Score: 182.06  E-value: 4.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  216 QSCTEILELQPSSVCVGEEFQIVLSGRGFMLGSRNGSVLCTYTVNETYTTSVKPVSVQLNSMLCPAPILNKAGETLDVSV 295
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 224809466  296 SFNGGKSVISGSLIVTATECSN 317
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
Ant_C pfam05586
Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic ...
 394-479 1.83e-48

Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic C-terminus of the anthrax receptor.


Pssm-ID: 461683  Cd Length: 93  Bit Score: 161.70  E-value: 1.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  394 VRWGDKGSTEEGARLEKAKNAVVKIPEETEEPIRPRPPRPKPTHQPPQTKWYTPIKGRLDALWALLRRQYDRVSLMRPQE 473
Cdd:pfam05586   1 VRWGEKGSTEEGAKLEKAKNAVVKMPEEEEEPPEPRPRKPPARKPPPQRKWYTPIKGKLDALWALLRRGYDRVSLMRPTP 80


                  ....*..
gi 224809466  474 GDE-VCI 479
Cdd:pfam05586  81 GDKgRCI 87
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 29-191 8.76e-20

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 89.39  E-value: 8.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  29 GLLRAQEQPSCRRAFDLYFVLDKSGSVANNWIEIynfVQQLAERFVS---PEMRLSFIVFSSQATIILPLT--GDRGKIs 103
Cdd:COG2304   78 GLQPPKAAAEERPPLNLVFVIDVSGSMSGDKLEL---AKEAAKLLVDqlrPGDRVSIVTFAGDARVLLPPTpaTDRAKI- 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466 104 kgLEDLKRVSPVGETYIHEGLKLANEQIQKAGGLKTSSIIIALTDGKLD-GLV-PSYAEKEAKISRSLGASVYCVGV-LD 180
Cdd:COG2304  154 --LAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANvGITdPEELLKLAEEAREEGITLTTLGVgSD 231

                        170
                 ....*....|.
gi 224809466 181 FEQAQLERIAD 191
Cdd:COG2304  232 YNEDLLERLAD 242
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 44-197 1.62e-19

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 85.97  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466    44 DLYFVLDKSGSVANNWIEIY-NFVQQLAERF--VSPEMRLSFIVFSSQATIILPL--TGDRGKISKGLEDLkRVSPVGET 118
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAkEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASL-SYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466   119 YIHEGLKLANEQI---QKAGGLKTSSIIIALTDGKLDGLvPSYAEKEAKISRSLGASVYCVGV-LDFEQAQLERIADSKE 194
Cdd:smart00327  80 NLGAALQYALENLfskSAGSRRGAPKVVILITDGESNDG-PKDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPG 158


                   ...
gi 224809466   195 QVF 197
Cdd:smart00327 159 GVY 161
VWA pfam00092
von Willebrand factor type A domain;
44-197 1.10e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 83.48  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466   44 DLYFVLDKSGSV-ANNWIEIYNFVQQLAERF-VSPE-MRLSFIVFSSQATIILPLTGDRGK--ISKGLEDLkRVSPVGET 118
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLdIGPDgTRVGLVQYSSDVRTEFPLNDYSSKeeLLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  119 YIHEGLKLANEQIQKA---GGLKTSSIIIALTDGKLDGlvpSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSKEQ 195
Cdd:pfam00092  80 NTGKALKYALENLFSSaagARPGAPKVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGE 156


                  ..
gi 224809466  196 VF 197
Cdd:pfam00092 157 GH 158
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 39-221 6.54e-110

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 323.31  E-value: 6.54e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  39 CRRAFDLYFVLDKSGSVANNWIEIYNFVQQLAERFVSPEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGET 118
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466 119 YIHEGLKLANEQI--QKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSKEQV 196
Cdd:cd01474   81 YIHEGLENANEQIfnRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|....*
gi 224809466 197 FPVKGGFQALKGIINSILAQSCTEI 221
Cdd:cd01474  161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 216-317 4.28e-56

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


Pssm-ID: 461684  Cd Length: 102  Bit Score: 182.06  E-value: 4.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  216 QSCTEILELQPSSVCVGEEFQIVLSGRGFMLGSRNGSVLCTYTVNETYTTSVKPVSVQLNSMLCPAPILNKAGETLDVSV 295
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 224809466  296 SFNGGKSVISGSLIVTATECSN 317
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
Ant_C pfam05586
Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic ...
 394-479 1.83e-48

Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic C-terminus of the anthrax receptor.


Pssm-ID: 461683  Cd Length: 93  Bit Score: 161.70  E-value: 1.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  394 VRWGDKGSTEEGARLEKAKNAVVKIPEETEEPIRPRPPRPKPTHQPPQTKWYTPIKGRLDALWALLRRQYDRVSLMRPQE 473
Cdd:pfam05586   1 VRWGEKGSTEEGAKLEKAKNAVVKMPEEEEEPPEPRPRKPPARKPPPQRKWYTPIKGKLDALWALLRRGYDRVSLMRPTP 80


                  ....*..
gi 224809466  474 GDE-VCI 479
Cdd:pfam05586  81 GDKgRCI 87
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 43-194 3.46e-26

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 104.30  E-value: 3.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  43 FDLYFVLDKSGSVAN-NWIEIYNFVQQLAERFVSPE--MRLSFIVFSSQATIILPLT--GDRGKISKGLEDLKRVSPVGe 117
Cdd:cd01450    1 LDIVFLLDGSESVGPeNFEKVKDFIEKLVEKLDIGPdkTRVGLVQYSDDVRVEFSLNdyKSKDDLLKAVKNLKYLGGGG- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224809466 118 TYIHEGLKLANEQI--QKAGGLKTSSIIIALTDGKLDGLvpSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSKE 194
Cdd:cd01450   80 TNTGKALQYALEQLfsESNARENVPKVIIVLTDGRSDDG--GDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 44-191 4.08e-20

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 87.24  E-value: 4.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  44 DLYFVLDKSGSVANNWIEI-YNFVQQLAERFV--SPEMRLSFIVFSSQATIILPLTGDRGK--ISKGLEDLKRvSPVGET 118
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKaKEALKALVSSLSasPPGDRVGLVTFGSNARVVLPLTTDTDKadLLEAIDALKK-GLGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224809466 119 YIHEGLKLANEQIQKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKIsRSLGASVYCVGV-LDFEQAQLERIAD 191
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAAREL-RKLGITVYTIGIgDDANEDELKEIAD 153
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 29-191 8.76e-20

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 89.39  E-value: 8.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  29 GLLRAQEQPSCRRAFDLYFVLDKSGSVANNWIEIynfVQQLAERFVS---PEMRLSFIVFSSQATIILPLT--GDRGKIs 103
Cdd:COG2304   78 GLQPPKAAAEERPPLNLVFVIDVSGSMSGDKLEL---AKEAAKLLVDqlrPGDRVSIVTFAGDARVLLPPTpaTDRAKI- 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466 104 kgLEDLKRVSPVGETYIHEGLKLANEQIQKAGGLKTSSIIIALTDGKLD-GLV-PSYAEKEAKISRSLGASVYCVGV-LD 180
Cdd:COG2304  154 --LAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANvGITdPEELLKLAEEAREEGITLTTLGVgSD 231

                        170
                 ....*....|.
gi 224809466 181 FEQAQLERIAD 191
Cdd:COG2304  232 YNEDLLERLAD 242
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-191 1.40e-19

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 88.46  E-value: 1.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466   4 ERSPARSPGSWLFPGLWLLVLSGPGGLLRAQEQPSCRRAFDLYFVLDKSGS-VANNWIEIynfVQQLAERFVS---PEMR 79
Cdd:COG1240   54 AGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSmAAENRLEA---AKGALLDFLDdyrPRDR 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  80 LSFIVFSSQATIILPLTGDRGKISKGLEDLKrvsPVGETYIHEGLKLANEQIQKAGGlKTSSIIIALTDGKLDGLVPSyA 159
Cdd:COG1240  131 VGLVAFGGEAEVLLPLTRDREALKRALDELP---PGGGTPLGDALALALELLKRADP-ARRKVIVLLTDGRDNAGRID-P 205

                        170       180       190
                 ....*....|....*....|....*....|....
gi 224809466 160 EKEAKISRSLGASVYCVGVLD--FEQAQLERIAD 191
Cdd:COG1240  206 LEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAE 239
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 44-197 1.62e-19

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 85.97  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466    44 DLYFVLDKSGSVANNWIEIY-NFVQQLAERF--VSPEMRLSFIVFSSQATIILPL--TGDRGKISKGLEDLkRVSPVGET 118
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAkEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASL-SYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466   119 YIHEGLKLANEQI---QKAGGLKTSSIIIALTDGKLDGLvPSYAEKEAKISRSLGASVYCVGV-LDFEQAQLERIADSKE 194
Cdd:smart00327  80 NLGAALQYALENLfskSAGSRRGAPKVVILITDGESNDG-PKDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPG 158


                   ...
gi 224809466   195 QVF 197
Cdd:smart00327 159 GVY 161
VWA pfam00092
von Willebrand factor type A domain;
44-197 1.10e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 83.48  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466   44 DLYFVLDKSGSV-ANNWIEIYNFVQQLAERF-VSPE-MRLSFIVFSSQATIILPLTGDRGK--ISKGLEDLkRVSPVGET 118
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLdIGPDgTRVGLVQYSSDVRTEFPLNDYSSKeeLLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  119 YIHEGLKLANEQIQKA---GGLKTSSIIIALTDGKLDGlvpSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSKEQ 195
Cdd:pfam00092  80 NTGKALKYALENLFSSaagARPGAPKVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGE 156


                  ..
gi 224809466  196 VF 197
Cdd:pfam00092 157 GH 158
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 44-196 2.04e-14

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 71.65  E-value: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  44 DLYFVLDKSGSVANNWIEIY-NFVQQLAERFVSPEM--------RLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSP 114
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITkNFVKRVAERFLKDYYrkdpagswRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDNLEY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466 115 VGE-TYIHEGLKLANEQIQKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSK 193
Cdd:cd01480   84 IGGgTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVGSQNEEPLSRIACDG 163


                 ...
gi 224809466 194 EQV 196
Cdd:cd01480  164 KSA 166
VWA_2 pfam13519
von Willebrand factor type A domain;
45-144 1.87e-13

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 66.16  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466   45 LYFVLDKSGSVANNWIEIYNF--VQQLAERFVS--PEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSpvGETYI 120
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLeaAKDAVLALLKslPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPKG--GGTNL 78

                          90       100
                  ....*....|....*....|....
gi 224809466  121 HEGLKLANEQIQKAGGLKTSSIII 144
Cdd:pfam13519  79 AAALQLARAALKHRRKNQPRRIVL 102
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 44-199 1.18e-11

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 63.02  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  44 DLYFVLDKSGSVA-NNWIEIYNFVQQLAERF-VSPE-MRLSFIVFSSQATIILPLTGDRGKISKgLEDLKRVSPVGE-TY 119
Cdd:cd01472    2 DIVFLVDGSESIGlSNFNLVKDFVKRVVERLdIGPDgVRVGVVQYSDDPRTEFYLNTYRSKDDV-LEAVKNLRYIGGgTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466 120 IHEGLKLANEQIQKAG---GLKTSSIIIALTDGKL--DGLVPSYAEKEAkisrslGASVYCVGVLDFEQAQLERIADSK- 193
Cdd:cd01472   81 TGKALKYVRENLFTEAsgsREGVPKVLVVITDGKSqdDVEEPAVELKQA------GIEVFAVGVKNADEEELKQIASDPk 154


                 ....*..
gi 224809466 194 -EQVFPV 199
Cdd:cd01472  155 eLYVFNV 161
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 2-191 2.57e-11

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 63.93  E-value: 2.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466   2 VAERSPARSPGSWLFPGLWLLVLSGPGGLLRAQEqpscRRAFDLYFVLDKSGSVANNWIEI-YNFVQQLAERFvSPEMRL 80
Cdd:COG2425   82 AALLDALLLAVLLLALLLLAALLLLAAPASAAVP----LLEGPVVLCVDTSGSMAGSKEAAaKAAALALLRAL-RPNRRF 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  81 SFIVFSSQATIILPLTGDRGkISKGLEDLKRVSPVGETYIHEGLKLANEQIQKAGGLKTssIIIALTDGKlDGLVPSYAE 160
Cdd:COG2425  157 GVILFDTEVVEDLPLTADDG-LEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRNA--DIVLITDGE-AGVSPEELL 232

                        170       180       190
                 ....*....|....*....|....*....|..
gi 224809466 161 KEAKiSRSLGASVYCVGVLDF-EQAQLERIAD 191
Cdd:COG2425  233 REVR-AKESGVRLFTVAIGDAgNPGLLEALAD 263
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 44-178 5.51e-11

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 61.63  E-value: 5.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  44 DLYFVLDKSGSVA-NNWieiYNFVQQLAERFV-----SP-EMRLSFIVFSSQATIILPLTG----DRGKISKGLEDLKRV 112
Cdd:cd01471    2 DLYLLVDGSGSIGySNW---VTHVVPFLHTFVqnlniSPdEINLYLVTFSTNAKELIRLSSpnstNKDLALNAIRALLSL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224809466 113 -SPVGETYIHEGLKLANEQIQKAGGLKTSSI--IIALTDGKLDGlvPSYAEKEAKISRSLGASVYCVGV 178
Cdd:cd01471   79 yYPNGSTNTTSALLVVEKHLFDTRGNRENAPqlVIIMTDGIPDS--KFRTLKEARKLRERGVIIAVLGV 145
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 45-192 7.31e-11

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 60.75  E-value: 7.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  45 LYFVLDKSGSVANNWIEIynfVQQLAERFVS---PEMRLSFIVFSSQATIILPLT--GDRGKISKGLEdlkRVSPVGETY 119
Cdd:cd01465    3 LVFVIDRSGSMDGPKLPL---VKSALKLLVDqlrPDDRLAIVTYDGAAETVLPATpvRDKAAILAAID---RLTAGGSTA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224809466 120 IHEGLKLANEQIQKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKI--SRSLGASVYCVGVLD-FEQAQLERIADS 192
Cdd:cd01465   77 GGAGIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVaqKRESGITLSTLGFGDnYNEDLMEAIADA 152
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 44-178 5.73e-09

VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 55.41  E-value: 5.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  44 DLYFVLDKSGSVANNWIEIYN---FVQQLAERFVS--PEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGET 118
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVKPSrleAAKEVLSDFIDrrENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLAGQGT 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224809466 119 YIHEGLKLANEQIQKAGGLktSSIIIALTDGK--LDGLVPsyaEKEAKISRSLGASVYCVGV 178
Cdd:cd01467   84 AIGDAIGLAIKRLKNSEAK--ERVIVLLTDGEnnAGEIDP---ATAAELAKNKGVRIYTIGV 140
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 44-197 1.00e-06

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 48.55  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  44 DLYFVLDKSGSVAnnwiEIYNFVQQLAERFVS-----PE-MRLSFIVFSSQAT----IILPLTGDRGKISKGLEDLKRVS 113
Cdd:cd01476    2 DLLFVLDSSGSVR----GKFEKYKKYIERIVEgleigPTaTRVALITYSGRGRqrvrFNLPKHNDGEELLEKVDNLRFIG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466 114 pvGETYIHEGLKLANEQIQKAGGLK--TSSIIIALTDGKLDGLVpsyaEKEAKISRSL-GASVYCVGVLD---FEQAQLE 187
Cdd:cd01476   78 --GTTATGAAIEVALQQLDPSEGRRegIPKVVVVLTDGRSHDDP----EKQARILRAVpNIETFAVGTGDpgtVDTEELH 151

                        170
                 ....*....|
gi 224809466 188 RIADSKEQVF 197
Cdd:cd01476  152 SITGNEDHIF 161
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
40-150 4.88e-06

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 47.23  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  40 RRAFDLYFVLDKSGSVANNWIEIYN-----FVQQL-AERFVSPEMRLSFIVFSSQATIILPLTgdrgkiskGLEDLK--R 111
Cdd:COG4245    3 MRRLPVYLLLDTSGSMSGEPIEALNeglqaLIDELrQDPYALETVEVSVITFDGEAKVLLPLT--------DLEDFQppD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 224809466 112 VSPVGETYIHEGLKLANEQIQKAGGLKTSS-------IIIALTDGK 150
Cdd:COG4245   75 LSASGGTPLGAALELLLDLIERRVQKYTAEgkgdwrpVVFLITDGE 120
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 44-150 5.56e-05

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 43.53  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809466  44 DLYFVLDKSGSVANNWIEIynfVQQlAERFV----SPEMRLSFIVFSSQATIILPLtgdRGKISKGLEDLKRV----SPV 115
Cdd:cd01466    2 DLVAVLDVSGSMAGDKLQL---VKH-ALRFVisslGDADRLSIVTFSTSAKRLSPL---RRMTAKGKRSAKRVvdglQAG 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 224809466 116 GETYIHEGLKLAneqIQKAGGLKTS---SIIIALTDGK 150
Cdd:cd01466   75 GGTNVVGGLKKA---LKVLGDRRQKnpvASIMLLSDGQ 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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